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Crystal structure of anthrolysin O (alo)

Analyse Crystal structure of anthrolysin O (alo) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CQF
Type
protein
Length
924 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thiol-activated cytolysin
UniProt
Q81N62
Pockets
9 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BThiol-activated cytolysinprotein46219% helix, 35% strandQ81N62

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11070.570.8520empty
21330.570.8324empty
31480.560.8227empty
41160.550.8321empty
5990.420.7722empty

Interfaces

1 interface between chains.

  • A–B · 436 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 3CQF · Crystal structure of anthrolysin O (ALO) · the same entry in another collection · chain A against A, TM-score 1.00

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